ID   A0A671V6I4_SPAAU        Unreviewed;       646 AA.
AC   A0A671V6I4;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   28-JUN-2023, entry version 14.
DE   SubName: Full=Caseinolytic mitochondrial matrix peptidase chaperone subunit {ECO:0000313|Ensembl:ENSSAUP00010022338.1};
GN   Name=clpx {ECO:0000313|Ensembl:ENSSAUP00010022338.1};
OS   Sparus aurata (Gilthead sea bream).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Sparus.
OX   NCBI_TaxID=8175 {ECO:0000313|Ensembl:ENSSAUP00010022338.1, ECO:0000313|Proteomes:UP000472265};
RN   [1] {ECO:0000313|Ensembl:ENSSAUP00010022338.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A671V6I4; -.
DR   Ensembl; ENSSAUT00010023590.1; ENSSAUP00010022338.1; ENSSAUG00010009850.1.
DR   GeneTree; ENSGT00390000017625; -.
DR   InParanoid; A0A671V6I4; -.
DR   OMA; HRSDFTN; -.
DR   Proteomes; UP000472265; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd19497; RecA-like_ClpX; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010603; Znf_CppX_C4.
DR   PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   TIGRFAMs; TIGR00382; clpX; 1.
DR   PROSITE; PS51902; CLPX_ZB; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472265};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          106..159
FT                   /note="ClpX-type ZB"
FT                   /evidence="ECO:0000259|PROSITE:PS51902"
FT   REGION          83..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  70829 MW;  BE3A06FA34E1546F CRC64;
     MCYELIKATV SCDLCRAATG CSISSFVDCF SVNQLIDSPF KGALCGFDED ILIRRESSSL
     THLIFHFFVS FSETAVCFAS KDGTTKDGGS DGGKKSISEG KRLSGSGGSG KGGSQLRCPK
     CGDPCTHVET FVSSTRFVKC EKCHHFFVVL SETDSKKGLN KEPESAAEAV KLAFAQKPPP
     PPKKIYAYLD KYVVGQSYAK KVLAVAVYNH YKRIYNNIPA GSRQQVEVEK QPSLTPRELE
     MRRREDEYRF TKLLQIAGIS PHGNALGASM QQQASQQAPQ EKRGGEVLDS THTEIKLEKS
     NIILLGPTGS GKTLLAQTLA RCLDVPFAIC DCTTLTQAGY VGEDIESVIA KLLQDANYSV
     EKAQQGIVFL DEVDKIGSVP GIHQLRDVGG EGVQQGLLKL LEGTIVNVPE KNSRKLRGET
     VQVDTTNILF VASGAFNGLD RIISRRKNEK YLGFGTPSNL GKGRRAAAAA DLANTSGETD
     TVAEIEEKDR LLKLVEARDL IEFGMIPEFV GRLPVVVPLH SLDEETLVRI LTEPRNAVVP
     QYQALFSMDK CELNVNQDAL RAIARMALER KTGARGLRSI MEKLLLEPMF EVPHSDIMAV
     ELDKDVVQGK SQPRYIRAPA KETAEEEYDS GIEEENWPRQ ADAANN
//